Isolation of a photoactive photosynthetic reaction center-core antenna complex from Heliobacillus mobilis

Trost, Jeffrey T.; Blankenship, Robert E.

doi:10.1021/bi00452a003

Cited by 117 publications

(139 citation statements)

References 39 publications

(51 reference statements)

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“…Such large differences have also been observed for the RC subunits of purple bacteria, Chlorobiaceae, C. aurantiacus, and of PSI. Ferguson plot analysis of the P800 RC polypeptide (12) suggests that it binds an anomalously high amount of SDS, similar to what has been found in PSI (16). Downstream of the RC gene is an ORF coding for a 197-amino acid residue protein (ORF-197) and preceded by a Shine-Dalgarno sequence.…”

Section: Resultssupporting

confidence: 61%

“…mobilis possesses a true molecular mass of 68 kDa. This value is considerably larger than the electrophoretically determined 47-kDa value (10,12). Such large differences have also been observed for the RC subunits of purple bacteria, Chlorobiaceae, C. aurantiacus, and of PSI.…”

Section: Resultsmentioning

confidence: 69%

“…The RC-antenna complex from Hb. mobilis was isolated and purified as described (12) and represented a single 47-kDa band on SDS/PAGE. Cleavage of the RC protein was performed chemically by cyanogen bromide and 2-(2'-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine and enzymatically by Clostripain.…”

Section: Methodsmentioning

confidence: 99%

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Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems.

Liebl

Mockensturm-Wilson

Trost

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

171

178

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The gene for a reaction center core polypeptide from the anoxygenic photosynthetic bacterium Heliobacillus mobilis was cloned and sequenced. The deduced amino acid sequence consists of 609 residues with a molecular mass of 68 kDa. An adjacent open reading frame is not transcribed under our experimental conditions. No evidence for a second related reaction center core gene was found. The primary sequence of the reaction center protein (P800 protein) shows a high percentage of sequence identity to photosystem I in a cysteine-containing loop, which is the putative binding site of the iron-sulfur center FX and in the preceding hydrophobic region. Our data imply a homodimeric organization of the reaction center. This is fundamentally different from photosystem I and most other photosynthetic reaction centers, where the reaction center core is composed of two similar but nonidentical subunits.

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Section: Resultssupporting

confidence: 61%

Section: Resultsmentioning

confidence: 69%

See 1 more Smart Citation

Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems.

Liebl

Mockensturm-Wilson

Trost

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

171

178

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“…Heliobacteria are photosynthetic bacteria that uniquely employ bacteriochlorophyll (Bchl) g as the major antenna pigment and primary electron donor within a type I reaction center (RC) (3,55). Bchl g is related to chlorophyll (Chl) a but has an ethylidine functional group at the C-8 1 position and is esterified with farnesol rather than phytol (33).…”

mentioning

confidence: 99%

The Genome of Heliobacterium modesticaldum , a Phototrophic Representative of the Firmicutes Containing the Simplest Photosynthetic Apparatus

et al. 2008

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Despite the fact that heliobacteria are the only phototrophic representatives of the bacterial phylum Firmicutes, genomic analyses of these organisms have yet to be reported. Here we describe the complete sequence and analysis of the genome of Heliobacterium modesticaldum, a thermophilic species belonging to this unique group of phototrophs. The genome is a single 3.1-Mb circular chromosome containing 3,138 open reading frames. As suspected from physiological studies of heliobacteria that have failed to show photoautotrophic growth, genes encoding enzymes for known autotrophic pathways in other phototrophic organisms, including ribulose bisphosphate carboxylase (Calvin cycle), citrate lyase (reverse citric acid cycle), and malyl coenzyme A lyase (3-hydroxypropionate pathway), are not present in the H. modesticaldum genome. Thus, heliobacteria appear to be the only known anaerobic anoxygenic phototrophs that are not capable of autotrophy. Although for some cellular activities, such as nitrogen fixation, there is a full complement of genes in H. modesticaldum, other processes, including carbon metabolism and endosporulation, are more genetically streamlined than they are in most other low-G؉C gram-positive bacteria. Moreover, several genes encoding photosynthetic functions in phototrophic purple bacteria are not present in the heliobacteria. In contrast to the nutritional flexibility of many anoxygenic phototrophs, the complete genome sequence of H. modesticaldum reveals an organism with a notable degree of metabolic specialization and genomic reduction.

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“…Its structure has not been resolved yet, although crystallization has been achieved (7,8). Interestingly, however, a similarity to the reaction center of green sulfur bacteria has been recognized (9)(10)(11)(12)(13)(14)(15). All the redox components known for PS1 (7,8), the "special pair" of chlorophylls as electron donor, A. and A1 as early electron acceptors, and the subsequent FeS centers X, A, and B, have also been detected in the green sulfur bacterium Chlorobium limicola (11,13), and they seem to exist as well in the distantly related Heliobacteria (14,16).…”

mentioning

confidence: 99%

Photosynthetic reaction center genes in green sulfur bacteria and in photosystem 1 are related.

Büttner

Xie

Nelson

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

200

113

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Oxygenic photosynthesis of chloroplasts and cyanobacteria involves two photosystems, which originate from different prokaryotic ancestors. The reaction center of photosystem 2 (PS2) is related to the well-characterized reaction center of purple bacteria, while the reaction center of photosystem 1 (PS1) is related to the green sulfur bacteria, as is convincingly documented here. An operon encoding the P840 reaction center of Chlorobium limicola f.sp. thiosulfatophilum has been cloned and sequenced. It contains two structural genes, coding for proteins of 730 and 232 amino acids. The first protein resembles the large subunits of the PS1 reaction center. Putative binding elements for the primary donor, P840 in Chlorobium and P700 in PS1, and for the acceptors A

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Isolation of a photoactive photosynthetic reaction center-core antenna complex from Heliobacillus mobilis

Cited by 117 publications

References 39 publications

Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems.

Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems.

The Genome of Heliobacterium modesticaldum , a Phototrophic Representative of the Firmicutes Containing the Simplest Photosynthetic Apparatus

Photosynthetic reaction center genes in green sulfur bacteria and in photosystem 1 are related.

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